dbPTM

EFTU_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EFTU_HUMAN
UniProt AC	P49411
Protein Name	Elongation factor Tu, mitochondrial
Gene Name	TUFM
Organism	Homo sapiens (Human).
Sequence Length	452
Subcellular Localization	Mitochondrion .
Protein Description	Promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Plays also a role in the regulation of autophagy and innate immunity. Recruits ATG5-ATG12 and NLRX1 at mitochondria and serves as a checkpoint of the RIG-I/DDX58-MAVS pathway. In turn, inhibits RLR-mediated type I interferon while promoting autophagy..
Protein Sequence	MAAATLLRATPHFSGLAAGRTFLLQGLLRLLKAPALPLLCRGLAVEAKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLAMTEEEKNIKWG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
32	Ubiquitination	QGLLRLLKAPALPLL HHHHHHHHCCHHHHH	57.84	-
35	Ubiquitination	LRLLKAPALPLLCRG HHHHHCCHHHHHHHH	27.03	-
51	Ubiquitination	AVEAKKTYVRDKPHV HHHHHHHCCCCCCCE	11.45	-
55	2-Hydroxyisobutyrylation	KKTYVRDKPHVNVGT HHHCCCCCCCEEEEE	26.85	-
55	Acetylation	KKTYVRDKPHVNVGT HHHCCCCCCCEEEEE	26.85	25953088
58	Ubiquitination	YVRDKPHVNVGTIGH CCCCCCCEEEEEEEE	9.35	-
62	Phosphorylation	KPHVNVGTIGHVDHG CCCEEEEEEEEECCC	21.36	27080861
65	Phosphorylation	VNVGTIGHVDHGKTT EEEEEEEEECCCHHH	20.27	-
70	2-Hydroxyisobutyrylation	IGHVDHGKTTLTAAI EEEECCCHHHHHHHH	34.61	-
71	Phosphorylation	GHVDHGKTTLTAAIT EEECCCHHHHHHHHH	31.46	20860994
72	Phosphorylation	HVDHGKTTLTAAITK EECCCHHHHHHHHHH	26.12	20860994
74	Phosphorylation	DHGKTTLTAAITKIL CCCHHHHHHHHHHHH	16.38	20068231
77	Phosphorylation	KTTLTAAITKILAEG HHHHHHHHHHHHHCC	3.60	20068231
78	Phosphorylation	TTLTAAITKILAEGG HHHHHHHHHHHHCCC	13.80	20068231
79	2-Hydroxyisobutyrylation	TLTAAITKILAEGGG HHHHHHHHHHHCCCC	29.61	-
79	Acetylation	TLTAAITKILAEGGG HHHHHHHHHHHCCCC	29.61	19608861
79	Ubiquitination	TLTAAITKILAEGGG HHHHHHHHHHHCCCC	29.61	21890473
82	Acetylation	AAITKILAEGGGAKF HHHHHHHHCCCCCCC	19.50	19608861
82	Ubiquitination	AAITKILAEGGGAKF HHHHHHHHCCCCCCC	19.50	19608861
88	Acetylation	LAEGGGAKFKKYEEI HHCCCCCCCCCHHHC	62.08	19608861
88	Succinylation	LAEGGGAKFKKYEEI HHCCCCCCCCCHHHC	62.08	23954790
88	Ubiquitination	LAEGGGAKFKKYEEI HHCCCCCCCCCHHHC	62.08	21890473
90	Acetylation	EGGGAKFKKYEEIDN CCCCCCCCCHHHCCC	54.46	23749302
90	Ubiquitination	EGGGAKFKKYEEIDN CCCCCCCCCHHHCCC	54.46	-
91	Acetylation	GGGAKFKKYEEIDNA CCCCCCCCHHHCCCC	62.11	25825284
91	Methylation	GGGAKFKKYEEIDNA CCCCCCCCHHHCCCC	62.11	-
91	Ubiquitination	GGGAKFKKYEEIDNA CCCCCCCCHHHCCCC	62.11	21906983
92	Phosphorylation	GGAKFKKYEEIDNAP CCCCCCCHHHCCCCC	21.27	29496907
94	Acetylation	AKFKKYEEIDNAPEE CCCCCHHHCCCCCHH	53.18	-
94	Methylation	AKFKKYEEIDNAPEE CCCCCHHHCCCCCHH	53.18	-
94	Ubiquitination	AKFKKYEEIDNAPEE CCCCCHHHCCCCCHH	53.18	21890473
95	Phosphorylation	KFKKYEEIDNAPEER CCCCHHHCCCCCHHH	3.10	-
102	Methylation	IDNAPEERARGITIN CCCCCHHHHCCEEEE	28.11	-
104	Methylation	NAPEERARGITINAA CCCHHHHCCEEEEHH	43.18	-
105	Methylation	APEERARGITINAAH CCHHHHCCEEEEHHH	22.02	-
107	O-linked_Glycosylation	EERARGITINAAHVE HHHHCCEEEEHHHHE	15.82	OGP
107	Methylation	EERARGITINAAHVE HHHHCCEEEEHHHHE	15.82	-
107	Phosphorylation	EERARGITINAAHVE HHHHCCEEEEHHHHE	15.82	27080861
115	Phosphorylation	INAAHVEYSTAARHY EEHHHHEHHHHHHHC	15.38	27080861
116	O-linked_Glycosylation	NAAHVEYSTAARHYA EHHHHEHHHHHHHCC	9.69	OGP
116	Phosphorylation	NAAHVEYSTAARHYA EHHHHEHHHHHHHCC	9.69	22210691
117	O-linked_Glycosylation	AAHVEYSTAARHYAH HHHHEHHHHHHHCCC	24.35	OGP
117	Phosphorylation	AAHVEYSTAARHYAH HHHHEHHHHHHHCCC	24.35	27080861
118	Phosphorylation	AHVEYSTAARHYAHT HHHEHHHHHHHCCCC	9.14	-
122	Phosphorylation	YSTAARHYAHTDCPG HHHHHHHCCCCCCCC	8.43	28152594
125	Phosphorylation	AARHYAHTDCPGHAD HHHHCCCCCCCCCHH	30.99	28152594
127	Glutathionylation	RHYAHTDCPGHADYV HHCCCCCCCCCHHHH	4.58	22555962
133	Phosphorylation	DCPGHADYVKNMITG CCCCCHHHHHHCCCC	17.69	28152594
147	Glutathionylation	GTAPLDGCILVVAAN CCCCCCCEEEEEEEC	1.86	22555962
179	Phosphorylation	GVEHVVVYVNKADAV CCEEEEEEEEHHHHC	6.16	28152594
182	Phosphorylation	HVVVYVNKADAVQDS EEEEEEEHHHHCCCH	37.28	-
191	Sulfoxidation	DAVQDSEMVELVELE HHCCCHHHHHHHHHH	3.08	21406390
204	Phosphorylation	LEIRELLTEFGYKGE HHHHHHHHHHCCCCC	41.72	-
207	Phosphorylation	RELLTEFGYKGEETP HHHHHHHCCCCCCCC	19.60	-
208	Phosphorylation	ELLTEFGYKGEETPV HHHHHHCCCCCCCCE	22.57	-
211	Phosphorylation	TEFGYKGEETPVIVG HHHCCCCCCCCEEEE	55.32	-
219	O-linked_Glycosylation	ETPVIVGSALCALEG CCCEEEECHHHHHCC	13.74	32119511
222	Glutathionylation	VIVGSALCALEGRDP EEEECHHHHHCCCCH	3.98	22555962
227	Methylation	ALCALEGRDPELGLK HHHHHCCCCHHHCHH	47.11	-
230	Methylation	ALEGRDPELGLKSVQ HHCCCCHHHCHHHHH	60.81	-
234	2-Hydroxyisobutyrylation	RDPELGLKSVQKLLD CCHHHCHHHHHHHHH	46.94	-
234	Acetylation	RDPELGLKSVQKLLD CCHHHCHHHHHHHHH	46.94	25953088
234	Malonylation	RDPELGLKSVQKLLD CCHHHCHHHHHHHHH	46.94	26320211
234	Succinylation	RDPELGLKSVQKLLD CCHHHCHHHHHHHHH	46.94	21906983
234	Ubiquitination	RDPELGLKSVQKLLD CCHHHCHHHHHHHHH	46.94	-
237	Ubiquitination	ELGLKSVQKLLDAVD HHCHHHHHHHHHHHH	37.46	21890473
238	Acetylation	LGLKSVQKLLDAVDT HCHHHHHHHHHHHHH	49.19	23954790
238	Ubiquitination	LGLKSVQKLLDAVDT HCHHHHHHHHHHHHH	49.19	21890473
241	Acetylation	KSVQKLLDAVDTYIP HHHHHHHHHHHHCCC	55.79	-
241	Ubiquitination	KSVQKLLDAVDTYIP HHHHHHHHHHHHCCC	55.79	21890473
245	Phosphorylation	KLLDAVDTYIPVPAR HHHHHHHHCCCCCHH	19.42	28152594
246	Phosphorylation	LLDAVDTYIPVPARD HHHHHHHCCCCCHHH	9.96	28152594
248	Phosphorylation	DAVDTYIPVPARDLE HHHHHCCCCCHHHCC	18.67	-
249	Phosphorylation	AVDTYIPVPARDLEK HHHHCCCCCHHHCCC	4.14	-
256	2-Hydroxyisobutyrylation	VPARDLEKPFLLPVE CCHHHCCCCCEEEEE	48.65	-
256	Acetylation	VPARDLEKPFLLPVE CCHHHCCCCCEEEEE	48.65	19608861
256	Malonylation	VPARDLEKPFLLPVE CCHHHCCCCCEEEEE	48.65	26320211
256	Succinylation	VPARDLEKPFLLPVE CCHHHCCCCCEEEEE	48.65	23954790
256	Ubiquitination	VPARDLEKPFLLPVE CCHHHCCCCCEEEEE	48.65	21890473
259	Acetylation	RDLEKPFLLPVEAVY HHCCCCCEEEEEEEE	7.78	19608861
259	Ubiquitination	RDLEKPFLLPVEAVY HHCCCCCEEEEEEEE	7.78	19608861
266	Phosphorylation	LLPVEAVYSVPGRGT EEEEEEEEECCCCCE	15.82	29978859
267	Phosphorylation	LPVEAVYSVPGRGTV EEEEEEEECCCCCEE	18.42	27050516
270	Phosphorylation	EAVYSVPGRGTVVTG EEEEECCCCCEEEEE	38.19	27251275
273	Phosphorylation	YSVPGRGTVVTGTLE EECCCCCEEEEEEEE	15.50	20068231
276	Phosphorylation	PGRGTVVTGTLERGI CCCCEEEEEEEECCE	21.80	28450419
278	Phosphorylation	RGTVVTGTLERGILK CCEEEEEEEECCEEC	18.97	28450419
281	Methylation	VVTGTLERGILKKGD EEEEEEECCEECCCC	40.33	-
281	Phosphorylation	VVTGTLERGILKKGD EEEEEEECCEECCCC	40.33	-
284	Methylation	GTLERGILKKGDECE EEEECCEECCCCCEE	5.37	-
286	Malonylation	LERGILKKGDECELL EECCEECCCCCEEEC	69.05	26320211
286	Succinylation	LERGILKKGDECELL EECCEECCCCCEEEC	69.05	27452117
286	Ubiquitination	LERGILKKGDECELL EECCEECCCCCEEEC	69.05	-
289	Ubiquitination	GILKKGDECELLGHS CEECCCCCEEECCCC	38.26	-
290	S-nitrosocysteine	ILKKGDECELLGHSK EECCCCCEEECCCCC	5.48	-
290	Glutathionylation	ILKKGDECELLGHSK EECCCCCEEECCCCC	5.48	22555962
290	S-nitrosylation	ILKKGDECELLGHSK EECCCCCEEECCCCC	5.48	22178444
290	S-palmitoylation	ILKKGDECELLGHSK EECCCCCEEECCCCC	5.48	21044946
296	Phosphorylation	ECELLGHSKNIRTVV CEEECCCCCCCHHHH	26.12	28985074
297	Acetylation	CELLGHSKNIRTVVT EEECCCCCCCHHHHH	51.20	25953088
297	Ubiquitination	CELLGHSKNIRTVVT EEECCCCCCCHHHHH	51.20	-
299	Phosphorylation	LLGHSKNIRTVVTGI ECCCCCCCHHHHHHH	4.49	24719451
300	Methylation	LGHSKNIRTVVTGIE CCCCCCCHHHHHHHH	30.75	-
300	Ubiquitination	LGHSKNIRTVVTGIE CCCCCCCHHHHHHHH	30.75	-
303	Methylation	SKNIRTVVTGIEMFH CCCCHHHHHHHHHHH	3.92	-
304	Phosphorylation	KNIRTVVTGIEMFHK CCCHHHHHHHHHHHH	28.27	23312004
307	Phosphorylation	RTVVTGIEMFHKSLE HHHHHHHHHHHHHHH	36.82	-
308	Sulfoxidation	TVVTGIEMFHKSLER HHHHHHHHHHHHHHH	3.94	21406390
311	2-Hydroxyisobutyrylation	TGIEMFHKSLERAEA HHHHHHHHHHHHHHC	45.53	-
311	Acetylation	TGIEMFHKSLERAEA HHHHHHHHHHHHHHC	45.53	26822725
311	Ubiquitination	TGIEMFHKSLERAEA HHHHHHHHHHHHHHC	45.53	21890473
312	Phosphorylation	GIEMFHKSLERAEAG HHHHHHHHHHHHHCC	27.22	28450419
314	Acetylation	EMFHKSLERAEAGDN HHHHHHHHHHHCCCH	57.86	-
314	Ubiquitination	EMFHKSLERAEAGDN HHHHHHHHHHHCCCH	57.86	21890473
315	Phosphorylation	MFHKSLERAEAGDNL HHHHHHHHHHCCCHH	42.92	24719451
342	Acetylation	RRGLVMVKPGSIKPH HCCEEEECCCCCCCC	26.09	23236377
342	Malonylation	RRGLVMVKPGSIKPH HCCEEEECCCCCCCC	26.09	26320211
345	Phosphorylation	LVMVKPGSIKPHQKV EEEECCCCCCCCCEE	35.65	27080861
345	Ubiquitination	LVMVKPGSIKPHQKV EEEECCCCCCCCCEE	35.65	-
347	Acetylation	MVKPGSIKPHQKVEA EECCCCCCCCCEEEE	37.84	25953088
347	Malonylation	MVKPGSIKPHQKVEA EECCCCCCCCCEEEE	37.84	26320211
347	Succinylation	MVKPGSIKPHQKVEA EECCCCCCCCCEEEE	37.84	27452117
351	Acetylation	GSIKPHQKVEAQVYI CCCCCCCEEEEEEEE	38.72	7705789
357	Phosphorylation	QKVEAQVYILSKEEG CEEEEEEEEEECCCC	5.53	28152594
360	Phosphorylation	EAQVYILSKEEGGRH EEEEEEEECCCCCCC	28.58	28152594
361	2-Hydroxyisobutyrylation	AQVYILSKEEGGRHK EEEEEEECCCCCCCC	57.23	-
361	Acetylation	AQVYILSKEEGGRHK EEEEEEECCCCCCCC	57.23	25953088
361	Malonylation	AQVYILSKEEGGRHK EEEEEEECCCCCCCC	57.23	26320211
361	Ubiquitination	AQVYILSKEEGGRHK EEEEEEECCCCCCCC	57.23	2190698
363	Phosphorylation	VYILSKEEGGRHKPF EEEEECCCCCCCCCC	71.35	-
364	Acetylation	YILSKEEGGRHKPFV EEEECCCCCCCCCCH	39.25	-
364	Ubiquitination	YILSKEEGGRHKPFV EEEECCCCCCCCCCH	39.25	21890473
382	Phosphorylation	MPVMFSLTWDMACRI HHHHHHHHHCEECEE	20.44	-
395	2-Hydroxyisobutyrylation	RIILPPEKELAMPGE EEECCCHHHHCCCCC	64.90	-
395	Acetylation	RIILPPEKELAMPGE EEECCCHHHHCCCCC	64.90	26051181
395	Ubiquitination	RIILPPEKELAMPGE EEECCCHHHHCCCCC	64.90	-
399	Sulfoxidation	PPEKELAMPGEDLKF CCHHHHCCCCCCCCC	7.38	21406390
405	Acetylation	AMPGEDLKFNLILRQ CCCCCCCCCEEEECC	44.52	30582599
405	Succinylation	AMPGEDLKFNLILRQ CCCCCCCCCEEEECC	44.52	23954790
405	Ubiquitination	AMPGEDLKFNLILRQ CCCCCCCCCEEEECC	44.52	-
418	2-Hydroxyisobutyrylation	RQPMILEKGQRFTLR CCCEEECCCCCEEEE	57.82	-
418	Acetylation	RQPMILEKGQRFTLR CCCEEECCCCCEEEE	57.82	19608861
418	Succinylation	RQPMILEKGQRFTLR CCCEEECCCCCEEEE	57.82	27452117
418	Ubiquitination	RQPMILEKGQRFTLR CCCEEECCCCCEEEE	57.82	-
421	Acetylation	MILEKGQRFTLRDGN EEECCCCCEEEECCC	34.87	19608861
421	Ubiquitination	MILEKGQRFTLRDGN EEECCCCCEEEECCC	34.87	19608861
423	Phosphorylation	LEKGQRFTLRDGNRT ECCCCCEEEECCCEE	24.07	24719451
426	Phosphorylation	GQRFTLRDGNRTIGT CCCEEEECCCEEECC	62.93	24719451
430	Phosphorylation	TLRDGNRTIGTGLVT EEECCCEEECCCCEE	27.97	21406692
433	Phosphorylation	DGNRTIGTGLVTNTL CCCEEECCCCEECCC	24.40	21406692
437	O-linked_Glycosylation	TIGTGLVTNTLAMTE EECCCCEECCCCCCH	27.77	32119511
437	Phosphorylation	TIGTGLVTNTLAMTE EECCCCEECCCCCCH	27.77	24114839
439	Phosphorylation	GTGLVTNTLAMTEEE CCCCEECCCCCCHHH	13.41	21406692
442	Sulfoxidation	LVTNTLAMTEEEKNI CEECCCCCCHHHHCC	5.65	21406390
443	Phosphorylation	VTNTLAMTEEEKNIK EECCCCCCHHHHCCC	34.34	21406692
446	Phosphorylation	TLAMTEEEKNIKWG- CCCCCHHHHCCCCC-	45.21	-
447	2-Hydroxyisobutyrylation	LAMTEEEKNIKWG-- CCCCHHHHCCCCC--	68.22	-
447	Acetylation	LAMTEEEKNIKWG-- CCCCHHHHCCCCC--	68.22	23954790
447	Succinylation	LAMTEEEKNIKWG-- CCCCHHHHCCCCC--	68.22	27452117
447	Ubiquitination	LAMTEEEKNIKWG-- CCCCHHHHCCCCC--	68.22	-
450	Acetylation	TEEEKNIKWG----- CHHHHCCCCC-----	56.08	-
450	Ubiquitination	TEEEKNIKWG----- CHHHHCCCCC-----	56.08	21890473

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of EFTU_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EFTU_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of EFTU_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL17_HUMAN	RPL17	physical	22939629
RL23_HUMAN	RPL23	physical	22939629
RL11_HUMAN	RPL11	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RL23A_HUMAN	RPL23A	physical	22939629
RL19_HUMAN	RPL19	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RL14_HUMAN	RPL14	physical	22939629
RL12_HUMAN	RPL12	physical	22939629
RL15_HUMAN	RPL15	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RL32_HUMAN	RPL32	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RL3_HUMAN	RPL3	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RT07_HUMAN	MRPS7	physical	22939629
RM17_HUMAN	MRPL17	physical	22939629
RM11_HUMAN	MRPL11	physical	22939629
NACA2_HUMAN	NACA2	physical	22939629
RM14_HUMAN	MRPL14	physical	22939629
RT14_HUMAN	MRPS14	physical	22939629
RM22_HUMAN	MRPL22	physical	22939629
RM04_HUMAN	MRPL4	physical	22939629
RM24_HUMAN	MRPL24	physical	22939629
RT05_HUMAN	MRPS5	physical	22939629
RM23_HUMAN	MRPL23	physical	22939629
PPT2_HUMAN	PPT2	physical	22939629
CAVN3_HUMAN	PRKCDBP	physical	22939629
RT10_HUMAN	MRPS10	physical	22939629
HS90A_HUMAN	HSP90AA1	physical	22939629
RM02_HUMAN	MRPL2	physical	22939629
PHB2_HUMAN	PHB2	physical	22939629
SFXN3_HUMAN	SFXN3	physical	22939629
SYSM_HUMAN	SARS2	physical	22939629
RM01_HUMAN	MRPL1	physical	22939629
SYIM_HUMAN	IARS2	physical	22939629
NENF_HUMAN	NENF	physical	22939629
SYUG_HUMAN	SNCG	physical	22939629
EGLN_HUMAN	ENG	physical	22939629
KAD2_HUMAN	AK2	physical	22939629
PYC_HUMAN	PC	physical	22939629
DCPS_HUMAN	DCPS	physical	22863883
G3P_HUMAN	GAPDH	physical	22863883
IPO9_HUMAN	IPO9	physical	22863883
ULA1_HUMAN	NAE1	physical	22863883
PA1B2_HUMAN	PAFAH1B2	physical	22863883
IPP2_HUMAN	PPP1R2	physical	22863883
PPP5_HUMAN	PPP5C	physical	22863883
PLPHP_HUMAN	PROSC	physical	22863883
TBB6_HUMAN	TUBB6	physical	22863883
AR6P1_HUMAN	ARL6IP1	physical	25416956
CKLF5_HUMAN	CMTM5	physical	25416956
FUND1_HUMAN	FUNDC1	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956
CHMP7_HUMAN	CHMP7	physical	26344197
OST48_HUMAN	DDOST	physical	26344197
HIP1R_HUMAN	HIP1R	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
XPO1_HUMAN	XPO1	physical	26344197
ZMYM6_HUMAN	ZMYM6	physical	28514442
RRF2M_HUMAN	GFM2	physical	28514442
IF2M_HUMAN	MTIF2	physical	28514442
MCCA_HUMAN	MCCC1	physical	28514442
GAB1_HUMAN	GAB1	physical	28514442
TRUA_HUMAN	PUS1	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610678	Combined oxidative phosphorylation deficiency 4 (COXPD4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EFTU_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79; LYS-88; LYS-256 ANDLYS-418, AND MASS SPECTROMETRY.	19608861 [Abstract]